Beta-glucosidase from the grape native yeast Debaryomyces vanrijiae: purification, characterization, and its effect on monoterpene content of a Muscat grape juice.
J Agric Food Chem
; 51(5): 1453-9, 2003 Feb 26.
Article
em En
| MEDLINE
| ID: mdl-12590497
ABSTRACT
Six hundred ten yeast colonies isolated from various vineyards in Chile were screened for the presence of a beta-glucosidase activity as well as the resistance to glucose and ethanol inhibition. Among them, Debaryomyces vanrijiae was found to produce high levels of an extracelular beta-glucosidase which was tolerant to glucose (K(i) = 439 mM) and ethanol inhibitions. The enzyme (designated DV-BG) was purified to apparent homogeneity, respectively, by gel filtration, ion-exchange, and chromatofocusing techniques. Its molecular weight was 100 000, and its pI 3.0, optimum pH, and temperature activities were 5.0 and 40 degrees C, respectively, and had a V(max) of 47.6 micromol min(-)(1) mg(-)(1) and a K(m) of 1.07 mM. The enzyme was active against different beta-d-glucosides including glucosidic flavor precursors. The disaccharidic flavor precursors were not substrates for the enzyme. When added to a Muscat grape juice, the concentration of several monoterpenes increased as the consequence of its hydrolytic activity.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ascomicetos
/
Bebidas
/
Beta-Glucosidase
/
Vitis
/
Monoterpenos
/
Frutas
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article